ID   A0A3N2PS63_9PEZI        Unreviewed;       797 AA.
AC   A0A3N2PS63;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Heat shock protein {ECO:0000313|EMBL:ROT37359.1};
GN   ORFNames=SODALDRAFT_334449 {ECO:0000313|EMBL:ROT37359.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT37359.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT37359.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT37359.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; ML119057; ROT37359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2PS63; -.
DR   STRING; 1314773.A0A3N2PS63; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000272025; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW   Stress response {ECO:0000313|EMBL:ROT37359.1}.
FT   DOMAIN          113..257
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          509..702
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          687..778
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          326..406
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   797 AA;  87930 MW;  20085B17700A8EE1 CRC64;
     MQARRHLISS ARRLAGPHSR SLRPLSRAIL TETATLRIAP LLPIVAVRNY ANGRGPHPPG
     GTHRMNLGGE PEKPALEQYG IDLTARAREG KLDPVIGRDS EIQRTIQILS RRTKNNPVLI
     GNAGTGKTAI LEGLALRIIR GDVPESIKNK RVISLDLGSL IAGAKFRGDF EERLKKVLEE
     VQKAGGQVIL FIDELHVLLG LGKAEGSIDA SNLLKPALAR GELQCCGATT LTEYRQIEKD
     VALARRFQPI MVNEPTVQDT ISILRGIKDK YEVHHGVRIT DGALVAAATY SNRYVTDRFL
     PDKAIDLMDE AASHLKLQHE SKPEDIMALD QKIMTIQIEL ESLRKEKDVA SRERREKLEG
     DLKKLQDEIA ELNVRWEKER AEIDAVKRAQ EELDKARVQL EMAQREGNFG RAGELRYSVI
     PMLEQKIPKD GQQNEGTLIH DAVTADDIAA VVSRITGIPV SKLTSGHIEK LVHMEDTLRE
     SVRGQDEAIR AVSNAVRLQR AGLSGDNRPL ASFFFLGPTG VGKTELCKKL AGFLFSTESA
     VVRFDMSEFQ EKHTISRLIG APSGYVGYED AGQLTEAVRR KPYAVLLFDE FEKAHRDISA
     LLLQVLDEGY LTDAQGHKVD FRNTIIVLTS NLGADILVGA NPSVPYTETE DGDVGPDVRK
     AVMDIVSSAY PPEFLNRIDS FIIFKRLALD AIRDIVDIRL RELQSRLEDR RITLQVPNDV
     RDWLAERGYD PRFGARPLNR LITNEIGNGL ADKIIQGDLK MGETAVVSIK EDGSGLVVTS
     AGPATAPSAE SAAEEAS
//